CHSSB_CAEEL
ID CHSSB_CAEEL Reviewed; 804 AA.
AC P45895; Q5NUN9; Q8IG00;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Chondroitin sulfate synthase mig-22;
DE EC=2.4.1.175;
DE AltName: Full=Abnormal cell migration;
DE AltName: Full=Chondroitin-polymerizing factor {ECO:0000303|PubMed:15485872};
DE Short=ChPF {ECO:0000303|PubMed:15485872};
DE AltName: Full=N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase 1;
DE EC=2.4.1.226;
GN Name=mig-22; Synonyms=pfc-1; ORFNames=PAR2.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15485872; DOI=10.1074/jbc.m409615200;
RA Izumikawa T., Kitagawa H., Mizuguchi S., Nomura K.H., Nomura K., Tamura J.,
RA Gengyo-Ando K., Mitani S., Sugahara K.;
RT "Nematode chondroitin polymerizing factor showing cell-/organ-specific
RT expression is indispensable for chondroitin synthesis and embryonic cell
RT division.";
RL J. Biol. Chem. 279:53755-53761(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=16982046; DOI=10.1016/j.ydbio.2006.08.037;
RA Suzuki N., Toyoda H., Sano M., Nishiwaki K.;
RT "Chondroitin acts in the guidance of gonadal distal tip cells in C.
RT elegans.";
RL Dev. Biol. 300:635-646(2006).
RN [5]
RP INTERACTION WITH SQV-5.
RX PubMed=17237233; DOI=10.1074/jbc.m611107200;
RA Kitagawa H., Izumikawa T., Mizuguchi S., Dejima K., Nomura K.H., Egusa N.,
RA Taniguchi F., Tamura J., Gengyo-Ando K., Mitani S., Nomura K., Sugahara K.;
RT "Expression of rib-1, a Caenorhabditis elegans homolog of the human tumor
RT suppressor EXT genes, is indispensable for heparan sulfate synthesis and
RT embryonic morphogenesis.";
RL J. Biol. Chem. 282:8533-8544(2007).
CC -!- FUNCTION: Has both beta-1,3-glucuronic acid and beta-1,4-N-
CC acetylgalactosamine transferase activity. Transfers glucuronic acid
CC (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-
CC GalNAc to the non-reducing end of the elongating chondroitin polymer
CC (By similarity). Required together with sqv-5 for the biosynthesis of
CC chondroitin (PubMed:15485872). Chondroitin is involved in organogenesis
CC of the vulva, maturation of the gonad, and neural development
CC (PubMed:15485872, PubMed:16982046). May have a specific role in unc-
CC 6/netrin-mediated dorsal guidance of gonadal distal tip cells
CC (PubMed:16982046). Glycosyltransferase activity is weak
CC (PubMed:15485872). {ECO:0000250|UniProtKB:Q8IZ52,
CC ECO:0000269|PubMed:15485872, ECO:0000269|PubMed:16982046,
CC ECO:0000303|PubMed:16982046}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-(beta-D-GalNAc-
CC (1->4)-beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-
CC beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] +
CC H(+) + UDP; Xref=Rhea:RHEA:20800, Rhea:RHEA-COMP:14058, Rhea:RHEA-
CC COMP:14059, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:138442, ChEBI:CHEBI:138443; EC=2.4.1.175;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)](n)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-
CC beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-
CC D-galactosamine = 3-O-([beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)](n+1)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-
CC (1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:55000, Rhea:RHEA-COMP:14060, Rhea:RHEA-COMP:14301,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:138444, ChEBI:CHEBI:138445; EC=2.4.1.175;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-
CC (1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-
CC glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:23428, Rhea:RHEA-COMP:12575,
CC Rhea:RHEA-COMP:14058, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132105, ChEBI:CHEBI:138442;
CC EC=2.4.1.226;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-([beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-
CC GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-
CC D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-
CC GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:54996,
CC Rhea:RHEA-COMP:14060, Rhea:RHEA-COMP:14061, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:138444,
CC ChEBI:CHEBI:138445; EC=2.4.1.226;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with sqv-5. {ECO:0000269|PubMed:17237233}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:16982046}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P45895-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P45895-2; Sequence=VSP_019778;
CC -!- TISSUE SPECIFICITY: Expressed in seam cells, the vulval epithelium and
CC in oocytes (at protein level). {ECO:0000269|PubMed:15485872,
CC ECO:0000269|PubMed:16982046}.
CC -!- DEVELOPMENTAL STAGE: Expressed in distal tip cells of the growing gonad
CC arms from L3 to the young adult stage (at protein level).
CC {ECO:0000269|PubMed:16982046}.
CC -!- DISRUPTION PHENOTYPE: Viable but sterile, with reversion of cytokinesis
CC during early embryogenesis. {ECO:0000269|PubMed:15485872,
CC ECO:0000269|PubMed:16982046}.
CC -!- SIMILARITY: Belongs to the chondroitin N-
CC acetylgalactosaminyltransferase family. {ECO:0000305}.
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DR EMBL; AB110823; BAD80738.1; -; mRNA.
DR EMBL; AB110824; BAD80739.1; -; mRNA.
DR EMBL; FO081577; CCD72535.1; -; Genomic_DNA.
DR EMBL; FO081577; CCD72536.1; -; Genomic_DNA.
DR PIR; S44860; S44860.
DR RefSeq; NP_498934.1; NM_066533.4. [P45895-1]
DR RefSeq; NP_871671.1; NM_181942.3.
DR AlphaFoldDB; P45895; -.
DR BioGRID; 41434; 2.
DR IntAct; P45895; 1.
DR STRING; 6239.PAR2.4a.2; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR EPD; P45895; -.
DR PaxDb; P45895; -.
DR PeptideAtlas; P45895; -.
DR PRIDE; P45895; -.
DR EnsemblMetazoa; PAR2.4a.1; PAR2.4a.1; WBGene00003253. [P45895-1]
DR EnsemblMetazoa; PAR2.4a.2; PAR2.4a.2; WBGene00003253. [P45895-1]
DR EnsemblMetazoa; PAR2.4a.3; PAR2.4a.3; WBGene00003253. [P45895-1]
DR EnsemblMetazoa; PAR2.4b.1; PAR2.4b.1; WBGene00003253. [P45895-2]
DR EnsemblMetazoa; PAR2.4b.2; PAR2.4b.2; WBGene00003253. [P45895-2]
DR EnsemblMetazoa; PAR2.4b.3; PAR2.4b.3; WBGene00003253. [P45895-2]
DR EnsemblMetazoa; PAR2.4b.4; PAR2.4b.4; WBGene00003253. [P45895-2]
DR GeneID; 176231; -.
DR KEGG; cel:CELE_PAR2.4; -.
DR CTD; 176231; -.
DR WormBase; PAR2.4a; CE00848; WBGene00003253; mig-22. [P45895-1]
DR WormBase; PAR2.4b; CE32699; WBGene00003253; mig-22. [P45895-2]
DR eggNOG; KOG3708; Eukaryota.
DR GeneTree; ENSGT01050000244857; -.
DR InParanoid; P45895; -.
DR OMA; FGSDYDW; -.
DR OrthoDB; 758579at2759; -.
DR PhylomeDB; P45895; -.
DR PRO; PR:P45895; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003253; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:WormBase.
DR GO; GO:0047238; F:glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0050510; F:N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IBA:GO_Central.
DR InterPro; IPR008428; Chond_GalNAc.
DR Pfam; PF05679; CHGN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..804
FT /note="Chondroitin sulfate synthase mig-22"
FT /id="PRO_0000065415"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..804
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..198
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:15485872"
FT /id="VSP_019778"
SQ SEQUENCE 804 AA; 91036 MW; C799999A4C4C6314 CRC64;
MVGGGRTGIH LLLGFLIGAA LALFFFSSTP SIDLTSSLAA FTSCQNQETE TNVLEPSALE
KGRVYKDLSE HWIVHQDDMP APPHNQDATP KVTRTRFAAT ELGTRERVMA AVMAESALAL
SINATLGRHV PRVHLFADSS RIDNDLAQLT NLSPYKLNGQ KTHSMVLGLL FNMTVHNNYD
WFLLAKDSTY INPFVLLRMI DTMNWNEPVV MGEAAEDGSG RCRLDTGMLL SQPAMHALMN
NRNACNNFAL AADDDQLAFE KCIQIATNLT CKPLHQGVRY EVWRGAERAD SPAAHDSIED
WKHSPAFKRA LAVPRLLSDA DASALHDYFV RVEMQRADRE IIKMEAELSR LAEQEARETG
EAISWPPALP PYAKPPNRYQ VSTWEYFTMT ELFRSEPNQN VRRLEGKDFD DVAEVVVAAR
QQVESEEPEL EFVQLRNGYR VFDPRRGMDY MVDLTYRKTV NEMPEVDNRF ESDNEAAHEE
SLKEIVVERR VHVSRMIAST QLMNQAPYVK EDTDVTVVIP VASEKDVLPA RKLLARQARL
CLFPTEEARK TRMVVAVFPL IESRSVTAIT NDMEELKRRC KRSLLETDVL PVHPAVSTEG
KGTAAAAALD DAVDRYGANT IYLLLSPHAD VQKEFFDRAR INTIKHYQVF FPVPFVEYHP
TISGMEMTEK EEKETPTEQA REAALSRLRD GVEPKRKRTL IVQKEHGRFD SQDFSCFAVY
GVDYVTARAK FGQNERRNDL ISAFLGQDSI HVLRAVEPTL RIRYHKRSCD MESIDTEDIA
RCLDSKKENV AAKDQLAKLL FHEK
